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Sökning: WFRF:(Hedenqvist Mikael S.)

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1.
  • Reddy, C. Nagendranatha, et al. (författare)
  • Review of microplastic degradation : Understanding metagenomic approaches for microplastic degrading organisms
  • 2023
  • Ingår i: Polymer testing. - : Elsevier BV. - 0142-9418 .- 1873-2348. ; 128, s. 108223-
  • Forskningsöversikt (refereegranskat)abstract
    • Environmental problems caused by plastic pollution are among the most pressing issues of our time. In recent years, metagenomics has become a powerful tool for understanding the microbial communities responsible for plastic biodegradation. In this review, recent developments and trends in metagenomics are discussed, and a comprehensive overview of the metagenomic methodology, analysis, and comparison of plastic-degrading bacteria is provided. In addition, the environmental consequences of plastic degradation are discussed, such as the impact on soil, water, and air quality, as well as the potential health risks posed by ingesting and inhaling microplastics. Possible solutions to the plastic degradation problem, such as using biodegradable materials and implementing recycling programs, are also explained. This review highlights the potential impact of metagenomics on the development of sustainable solutions to plastic pollution.
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2.
  • Sanandaji, Nima, et al. (författare)
  • Unusual crystals of poly(epsilon-caprolactone) by unusual crystallisation : The effects of rapid cooling and fast solvent loss on the morphology, crystal structure and melting
  • 2013
  • Ingår i: Polymer. - : Elsevier BV. - 0032-3861 .- 1873-2291. ; 54:5, s. 1497-1503
  • Tidskriftsartikel (refereegranskat)abstract
    • The lateral habit, unit cell structure and melting behaviour of single crystals of poly(epsilon-caprolactone) (PCL) prepared by the rapid expansion of a supercritical solution technique was studied by AFM at ambient and higher temperatures and by grazing-incident X-ray scattering using a synchrotron source. After dissolving PCL in a solution of supercritical CO2 and 0.1 vol.% chloroform, an extremely fast phase transfer from a supercritical to a gas-like state occurred during expansion into atmospheric conditions, leading to a temporary temperature drop to below -;50 degrees C at the silica surface where the crystals were deposited. Single crystals of a hitherto unreported rectangular lateral habit were observed. Six-sided crystals were also observed, but they were fewer than the rectangular crystals and in addition the angles between the lateral faces were different from the theoretical angles between adjacent {110} faces and {110} and {100} faces. X-ray scattering indicated a polymorphic structure also including the orthorhombic (110) and (200) diffraction peaks. Distinct low angle peaks essentially along the c-axis indicated a stacking on a very fine scale (3.7-4.7 nm) within the crystals. The equatorial diffraction peaks indicated a less dense packing of the PCL stems. Rectangular single crystals with a height according to AFM of 11-27 nm melted between 40 and 45 degrees C, which is lower than the melting points (55 degrees C) recorded for the distorted six-sided crystals. The unusual conditions for crystallisation used gave the polymer molecules a severe limitation to rearrange from the initial random coil state. The facetted crystals consisted of a stack of 4 nm thick blocks; these blocks most probably constituted a regular variation in molecular packing, i.e. molecular order. The pronounced changes in the angles between adjacent faces from those observed in mature PCL crystals and the wide-angle X-ray scattering data indicated the presence of conformational disorder in the crystals.
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6.
  • Johansson, Kenth S., et al. (författare)
  • Surface modification of wheat gluten films for improved water resistance
  • 2010
  • Ingår i: Abstracts of Papers of the American Chemical Society. - : American Chemical Society (ACS). - 0065-7727. ; 240
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • Renewable packaging materials are of interest for a more sustainable environment, and wheat gluten (WG) is one of the most interesting candidates to replace petroleum-based oxygen-barrier polymers for packaging applications. This is due to its attractive combination of flexibility and strength, high gas (especially O2) barrier properties under low humidity conditions and renewability. The main drawback of WG, as with most biopolymers, is its water and moisture sensitivity. The aim of this study was therefore to improve the hydrophobicity of WG films by means of surface modification while maintaining the excellent O2 barrier properties. The surface modification work included a combination of electrospinning of WG fibers and different plasma surface modifications. The latter involved He plasma treatment for crosslinking the WG film prior to the deposition of electrospun WG fibers, O2/Ar plasma etching of the WG films with and without electrospun WG fibers for increasing the surface roughness, and plasma polymerization of hexamethyldisiloxane (HMDSO) and other hydrophobic precursors for hydrophobicity. The plasma polymerization trials were performed both at reduced and atmospheric pressure conditions. The aim of the combined work was to maximize the hydrophobicity by combining a suitable nano-microstructure of the WG fibers with the hydrophobicity of the plasma-deposited coatings. The surface modification work was mainly evaluated by means of water contact angle measurements (hydrophobicity), Scanning Electron Microscopy (surface structures), Water Vapor Transmission Rate (WVTR) (moisture barrier) and Oxygen Transmission Rate (OTR) measurements (oxygen barrier). The surface modification work resulted in significantly improved hydrophobic properties of the WG films. The initial water contact angle increased from 65 to 110-130 degrees, depending on the combinations of electrospinning and plasma modification conditions. The plasma coatings prepared at ambient conditions resulted in slightly lower contact angles compared the plasma coating prepared at reduced pressure. The WVTR and OTR measurements are still in progress and will be reported at the meeting.  
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7.
  • Kuktaite, Ramune, et al. (författare)
  • Monitoring Nanostructure Dynamics and Polymerization in Glycerol Plasticized Wheat Gliadin and Glutenin Films : Relation to Mechanical Properties
  • 2016
  • Ingår i: ACS Sustainable Chemistry and Engineering. - : American Chemical Society (ACS). - 2168-0485. ; 4:6, s. 2998-3007
  • Tidskriftsartikel (refereegranskat)abstract
    • Gliadin and glutenin proteins with 10, 20, 30 and 40% of glycerol were compression molded into films (130 °C) and evaluated for protein polymerization, β-sheet structure and nano-structural morphology. Here, for the first time we show how different amounts of glycerol impact the nano-structure and functional properties of the gliadin and glutenin films. Most polymerized protein was found in the gliadin films with 20 and 30% glycerol, and in all the glutenin films (except 10%), by RP-HPLC. A β-sheet-rich protein structure was found to be high in the 10 and 20% glycerol gliadin films, and in the 20 and 30% glycerol glutenin films by FT-IR. Glycerol content of 20, 30 and 40% impacted the nano-structural morphology of the gliadin glycerol films observed by SAXS, and to a limited extent for 10 and 20% glycerol gliadin films revealed by WAXS. No ordered nano-structure was found for the glutenin glycerol films. The 20%, 30% and 40% glycerol films were the most tunable for specific mechanical properties. For the highest stiffness and strength, the 10% glycerol protein films were the best choice.
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8.
  • Muneer, Faraz, et al. (författare)
  • Innovative Gliadin/Glutenin and Modified Potato Starch Green Composites : Chemistry, Structure, and Functionality Induced by Processing
  • 2016
  • Ingår i: ACS Sustainable Chemistry and Engineering. - : American Chemical Society (ACS). - 2168-0485. ; 4:12, s. 6332-6343
  • Tidskriftsartikel (refereegranskat)abstract
    • In this study, we combined two wheat proteins, gliadin (Gli)/glutenin (GT), and modified potato starch (MPS) into composites using extrusion. In the Gli/GT MPS composites, we studied the structural dynamics of proteins and starch, protein starch interactions, protein properties, and composite morphology in relation to mechanical and barrier properties. Materials with different ratios of Gli/GT and MPS were extruded using either glycerol or glycerol water at 110 and 130 degrees C. For the first time, a hierarchical hexagonal structure of Gli proteins was observed in Gli MPS composite at both extrusion temperatures. The higher temperature (130 degrees C) induced a higher degree of protein cross-links, an increase in the polymer size, and formation of beta-sheets compared to 110 degrees C. The combination of plasticizers (glycerol and water) favored a micro-structural morphology with improved gelatinization of starch, processability, as well as strength, stiffness, and extensibility of GT MPS composites. The highest amount of the oxidized proteins was observed in the samples with the highest protein content and at high extrusion temperature. The Gli- and GT MPS (30/70) samples showed promising oxygen barrier properties under ambient testing conditions. These findings provide in-depth information for tailoring the structural functional relationship of the Gli/GT-potato starch composites for their promising use in designing various green materials.
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9.
  • Plackett, David, et al. (författare)
  • Physical Properties and Morphology of Films Prepared from Microfibrillated Cellulose and Microfibrillated Cellulose in Combination with Amylopectin
  • 2010
  • Ingår i: Journal of Applied Polymer Science. - : Wiley. - 0021-8995 .- 1097-4628. ; 117:6, s. 3601-3609
  • Tidskriftsartikel (refereegranskat)abstract
    • Two types of microfibrillated cellulose (MFC) were prepared using either a sulfite pulp containing a high amount of hemicellulose (MFC 1) or a carboxymethylated dissolving pulp (MFC 2). MFC gels were then combined with amylopectin solutions to produce solvent-cast MFC-reinforced amylopectin films. Tensile testing revealed that MFC 2-reinforced films exhibited a more ductile behavior and that MFC 1-reinforced films had higher modulus of elasticity (E-modulus) at MFC loadings of 50 wt % or higher. Pure MFC films had relatively low oxygen permeability values when data were compared with those for a variety of other polymer films. MFC 1 and MFC 2 films had similar opacity but differences in appearance which were attributed to the presence of some larger fibers and nanofiber agglomerates in MFC 2. Field emission scanning electron microscopy (FE-SEM) and atomic force microscopy (AFM) were used to illustrate the morphology of MFC nanofibers in pure films and in an amylopectin matrix.
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10.
  • Rasheed, Faiza, et al. (författare)
  • Structural architecture and solubility of native and modified gliadin and glutenin proteins : non-crystalline molecular and atomic organization
  • 2014
  • Ingår i: RSC Advances. - 2046-2069. ; 4:4, s. 2051-2060
  • Tidskriftsartikel (refereegranskat)abstract
    • Wheat gluten (WG) and its components, gliadin and glutenin proteins, form the largest polymers in nature, which complicates the structural architecture of these proteins. Wheat gluten, gliadin and glutenin proteins in unmodified form showed few secondary structural features. Structural modification of these proteins using heat, pressure and the chemical chaperone glycerol resulted in a shift to organized structure. In modified gliadin, nano-structural molecular arrangements in the form of hexagonal closed packed (HCP) assemblies with lattice parameter of (58 angstrom) were obvious together with development of intermolecular disulphide bonds. Modification of glutenin resulted in highly polymerized structure with proteins linked not only by disulphide bonds, but also with other covalent and irreversible bonds, as well as the highest proportion of beta-sheets. From a combination of experimental evidence and protein algorithms, we have proposed tertiary structure models of unmodified and modified gliadin and glutenin proteins. An increased understanding of gliadin and glutenin proteins structure and behavior are of utmost importance to understand the applicability of these proteins for various applications including plastic materials, foams, adhesives, films and coatings.
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